Role of the conserved aspartate and phenylalanine residues in prokaryotic and mitochondrial elongation factor Ts in guanine nucleotide exchange

[摘要]

The guanine nucleotide exchange reaction catalyzed by elongation factor Ts is proposed to arise from the intrusion of the side chains of D80 and F81 near the Mg²⁺ binding site in EF-Tu. D80A and F81A mutants of E. coli EF-Ts were 2–3-fold less active in promoting GDP exchange with E. coli EF-Tu while the D80AF81A mutant was nearly 10-fold less active. The D84 and F85 mutants of EF-Ts_mt were 5–10-fold less active in stimulating the activity of EF-Tu_mt. The double mutation completely abolished the activity of EF-Ts_mt.

[学科分类] 生物化学/生物物理

[关键词] Protein synthesis;Elongation factor;Mitochondria;Elongation factor Tu;Elongation factor Ts